6g0b: Difference between revisions
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<StructureSection load='6g0b' size='340' side='right' caption='[[6g0b]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='6g0b' size='340' side='right' caption='[[6g0b]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6g0b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G0B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G0B FirstGlance]. <br> | <table><tr><td colspan='2'>[[6g0b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tertt Tertt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G0B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G0B FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6g00|6g00]], [[6g09|6g09]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6g00|6g00]], [[6g09|6g09]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TERTU_4506 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=377629 TERTT])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6g0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g0b OCA], [http://pdbe.org/6g0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g0b RCSB], [http://www.ebi.ac.uk/pdbsum/6g0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g0b ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6g0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g0b OCA], [http://pdbe.org/6g0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g0b RCSB], [http://www.ebi.ac.uk/pdbsum/6g0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g0b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The biological conversion of lignocellulosic matter into high-value chemicals or biofuels is of increasing industrial importance as the sector slowly transitions away from nonrenewable sources. Many industrial processes involve the use of cellulolytic enzyme cocktails - a selection of glycoside hydrolases and, increasingly, polysaccharide oxygenases - to break down recalcitrant plant polysaccharides. ORFs from the genome of Teredinibacter turnerae, a symbiont hosted within the gills of marine shipworms, were identified in order to search for enzymes with desirable traits. Here, a putative T. turnerae glycoside hydrolase from family 8, hereafter referred to as TtGH8, is analysed. The enzyme is shown to be active against beta-1,4-xylan and mixed-linkage (beta-1,3,beta-1,4) marine xylan. Kinetic parameters, obtained using high-performance anion-exchange chromatography with pulsed amperometric detection and 3,5-dinitrosalicyclic acid reducing-sugar assays, show that TtGH8 catalyses the hydrolysis of beta-1,4-xylohexaose with a kcat/Km of 7.5 x 10(7) M(-1) min(-1) but displays maximal activity against mixed-linkage polymeric xylans, hinting at a primary role in the degradation of marine polysaccharides. The three-dimensional structure of TtGH8 was solved in uncomplexed and xylobiose-, xylotriose- and xylohexaose-bound forms at approximately 1.5 A resolution; the latter was consistent with the greater kcat/Km for hexasaccharide substrates. A (2,5)B boat conformation observed in the -1 position of bound xylotriose is consistent with the proposed conformational itinerary for this class of enzyme. This work shows TtGH8 to be effective at the degradation of xylan-based substrates, notably marine xylan, further exemplifying the potential of T. turnerae for effective and diverse biomass degradation. | |||
Structure and function of a glycoside hydrolase family 8 endoxylanase from Teredinibacter turnerae.,Fowler CA, Hemsworth GR, Cuskin F, Hart S, Turkenburg J, Gilbert HJ, Walton PH, Davies GJ Acta Crystallogr D Struct Biol. 2018 Oct 1;74(Pt 10):946-955. doi:, 10.1107/S2059798318009737. Epub 2018 Oct 2. PMID:30289404<ref>PMID:30289404</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6g0b" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Tertt]] | |||
[[Category: Davies, G J]] | [[Category: Davies, G J]] | ||
[[Category: Fowler, C A]] | [[Category: Fowler, C A]] | ||
Latest revision as of 11:39, 17 October 2018
Crystal Structure of a GH8 xylotriose complex from Teredinibacter TurneraeCrystal Structure of a GH8 xylotriose complex from Teredinibacter Turnerae
Structural highlights
Publication Abstract from PubMedThe biological conversion of lignocellulosic matter into high-value chemicals or biofuels is of increasing industrial importance as the sector slowly transitions away from nonrenewable sources. Many industrial processes involve the use of cellulolytic enzyme cocktails - a selection of glycoside hydrolases and, increasingly, polysaccharide oxygenases - to break down recalcitrant plant polysaccharides. ORFs from the genome of Teredinibacter turnerae, a symbiont hosted within the gills of marine shipworms, were identified in order to search for enzymes with desirable traits. Here, a putative T. turnerae glycoside hydrolase from family 8, hereafter referred to as TtGH8, is analysed. The enzyme is shown to be active against beta-1,4-xylan and mixed-linkage (beta-1,3,beta-1,4) marine xylan. Kinetic parameters, obtained using high-performance anion-exchange chromatography with pulsed amperometric detection and 3,5-dinitrosalicyclic acid reducing-sugar assays, show that TtGH8 catalyses the hydrolysis of beta-1,4-xylohexaose with a kcat/Km of 7.5 x 10(7) M(-1) min(-1) but displays maximal activity against mixed-linkage polymeric xylans, hinting at a primary role in the degradation of marine polysaccharides. The three-dimensional structure of TtGH8 was solved in uncomplexed and xylobiose-, xylotriose- and xylohexaose-bound forms at approximately 1.5 A resolution; the latter was consistent with the greater kcat/Km for hexasaccharide substrates. A (2,5)B boat conformation observed in the -1 position of bound xylotriose is consistent with the proposed conformational itinerary for this class of enzyme. This work shows TtGH8 to be effective at the degradation of xylan-based substrates, notably marine xylan, further exemplifying the potential of T. turnerae for effective and diverse biomass degradation. Structure and function of a glycoside hydrolase family 8 endoxylanase from Teredinibacter turnerae.,Fowler CA, Hemsworth GR, Cuskin F, Hart S, Turkenburg J, Gilbert HJ, Walton PH, Davies GJ Acta Crystallogr D Struct Biol. 2018 Oct 1;74(Pt 10):946-955. doi:, 10.1107/S2059798318009737. Epub 2018 Oct 2. PMID:30289404[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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